Structure of PDB 3qtp Chain B

Receptor sequence

>3qtpB (length=439) Species: 5759 (Entamoeba histolytica)

LGSMSIQKVHAREILDSRGNPTIEVEITTGKGMFRSCVPSGASTGVHEAV
ELRDGDKKRYGGKGVLKAVENVNTIIGPALLGKNVLNQAELDEMMIKLDG
TNNKGKLGANAILGCSMSICRAAAAEKGLPLYKYLAELTGHKEMTMPVPC
FNVINGGAHAGNALAMQEFMICPTGATNFHEALRMAAETYQCLKVVIKAK
YGQDATNVGDEGGFAPNVSGAREALDLLVEAIAKAGYTGKIEIAMDCAAS
EFYNEETKKYDLGKKIPADKKDPSLVKDVDGLIAEYVDYGKHYPIASIED
PFAEDDWAAWNKFTVEHGNFQIVGDDLLVTNPARVQMAMDKNACNSVLIK
VNQIGTLTETFKTIKMAQEKGWGVMASHRSGETEDTFIADLVVGLNCKQI
KTGAPCRSERLCKYNQLMRIEEELGNIPYAGKNWRNSTA

3D structure

• PDB: 3qtp Structure analysis of Entamoeba histolytica enolase.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S40 H156 E165 E208 D243 E296 D322 K347 H375 K398
• Catalytic site (residue number reindexed from 1): S43 H159 E168 E211 D246 E299 D325 K350 H378 K401
• Enzyme Commision number: 4.2.1.11: phosphopyruvate hydratase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	2PG	B	G38 E165 E208 K347 H375 R376 K398	G41 E168 E211 K350 H378 R379 K401
BS02	MG	B	D243 E296 D322	D246 E299 D325

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004634 phosphopyruvate hydratase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006096 glycolytic process

Cellular Component

• GO:0000015 phosphopyruvate hydratase complex
• GO:0005634 nucleus
• GO:0005737 cytoplasm

External links

• PDB: RCSB:3qtp, PDBe:3qtp, PDBj:3qtp
• PDBsum: 3qtp
• PubMed: 21697600
• UniProt: P51555|ENO_ENTH1 Enolase 1 (Gene Name=ENO)